Biomolecular NMR Assignments

, Volume 6, Issue 1, pp 5–8 | Cite as

NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1

  • Joshua S. Mylne
  • Caroline Mas
  • Justine M. Hill


VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39 kDa protein comprised of two B3 domains flanking a putative nuclear localization sequence and two PEST domains. Here we report the 1H, 13C and 15N resonance assignments of the 134 residue C-terminal region of VRN1, comprising a B3 DNA binding domain of the REM family and an upstream region that is highly conserved among VRN1 homologs from other dicotyledonous plant species.


Vernalization B3 domain DNA binding Transcription factor Arabidopsis 



We thank Caroline Dean and Stéphane Mesnage for providing the VRN1 cDNA, and the Queensland NMR Network for measurement time on the 900 MHz NMR spectrometer. This work was supported by a University of Queensland Early Career Researcher Grant (2007/002133) to JSM and an Australian National Health and Medical Research Council RD Wright Fellowship (401748) to JMH. JSM is an Australian Research Council Queen Elizabeth II Fellow (DP0879133) and Caroline Mas is a University of Queensland Postdoctoral Research Fellow.


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Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Joshua S. Mylne
    • 1
  • Caroline Mas
    • 2
    • 3
  • Justine M. Hill
    • 2
    • 3
  1. 1.Institute for Molecular BioscienceThe University of QueenslandBrisbaneAustralia
  2. 2.School of Chemistry and Molecular BiosciencesThe University of QueenslandBrisbaneAustralia
  3. 3.Centre for Advanced ImagingThe University of QueenslandBrisbaneAustralia

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